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    Characterization of anti-myosin monoclonal antibodies.

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    Authors
    Nelson, Paul N.
    Astley, S.J.
    Roden, Denise A.
    Waldron, E.E.
    Baig, K.M.
    Caforio, A.L.
    Koutedakis, Yiannis
    Perera, Shantha
    Spry, C.
    Issue Date
    2005
    
    Metadata
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    Abstract
    The characterization of monoclonal antibodies (MAbs) with regard to reactivity and specificity is important for the successful application as a molecular probe and/or diagnostic reagent. Furthermore, it is recognized that some monoclonal reagents perform well in some assay systems but not others. In this study, the reactivity profiles of two anti-myosin MAbs (H1 and DH2, raised against human cardiac myosin) were evaluated in enzyme-linked immunosorbent assay (ELISA), slot-blotting, and immunocytochemistry. Both antibodies performed well in slot-blotting against myosin heavy chain preparations from cardiac and skeletal muscle and from non-human sources. In general, MAb H1 demonstrated strong to moderate reactivity in all assay systems, whilst MAb DH2 faired poorly in ELISA. MAb H1 also showed reactivity to synthetic peptides of myosin, one of which possessed a motif (ERRDA, single amino acid code) that was found in other human and nonhuman myosin protein sequences that could explain its cross-reactive profile. Intriguingly, this motif was found on viral and other pathogenic agents associated with myocarditis. Hence, it is speculated that this region could give some credence to the mechanism of molecular mimicry associated with some cardiac diseases. Overall, MAb H1 may serve as a useful probe of myosin structure.
    Citation
    Hybridoma, 24(6): 314-318
    Publisher
    New Rochelle (NY): Mary Ann Liebert, Inc.
    Journal
    Hybridoma
    URI
    http://hdl.handle.net/2436/30202
    DOI
    10.1089/hyb.2005.24.314
    PubMed ID
    16332199
    Additional Links
    https://www.liebertpub.com/doi/abs/10.1089/hyb.2005.24.314
    Type
    Journal article
    Language
    en
    ISSN
    1554-0014
    ae974a485f413a2113503eed53cd6c53
    10.1089/hyb.2005.24.314
    Scopus Count
    Collections
    Research Institute in Healthcare Science

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